Platelet-VWF complexes get the chop
In this issue of Blood, Shim and colleagues define a dual role for platelet glycoprotein (GP)Iba (the major ligand-binding subunit of the GPIb-IX-V complex) in regulating ADAMTS13-mediated cleavage of von Willebrand factor (VWF) under shear: it alleviates an inhibitory effect of the VWFA1 domain on...
| Main Authors: | , |
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| Format: | Journal Article |
| Published: |
American Society of Hematology
2008
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| Online Access: | http://hdl.handle.net/20.500.11937/45221 |
| _version_ | 1848757222814777344 |
|---|---|
| author | Berndt, Michael Andrews, R. |
| author_facet | Berndt, Michael Andrews, R. |
| author_sort | Berndt, Michael |
| building | Curtin Institutional Repository |
| collection | Online Access |
| description | In this issue of Blood, Shim and colleagues define a dual role for platelet glycoprotein (GP)Iba (the major ligand-binding subunit of the GPIb-IX-V complex) in regulating ADAMTS13-mediated cleavage of von Willebrand factor (VWF) under shear: it alleviates an inhibitory effect of the VWFA1 domain on cleavage of the A2 domain, 1 and it allows tensile force to be exerted on the A2 domain through at least 2 platelets binding per VWF multimer via the A1 domain (see figure). |
| first_indexed | 2025-11-14T09:24:40Z |
| format | Journal Article |
| id | curtin-20.500.11937-45221 |
| institution | Curtin University Malaysia |
| institution_category | Local University |
| last_indexed | 2025-11-14T09:24:40Z |
| publishDate | 2008 |
| publisher | American Society of Hematology |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | curtin-20.500.11937-452212017-09-13T14:19:38Z Platelet-VWF complexes get the chop Berndt, Michael Andrews, R. In this issue of Blood, Shim and colleagues define a dual role for platelet glycoprotein (GP)Iba (the major ligand-binding subunit of the GPIb-IX-V complex) in regulating ADAMTS13-mediated cleavage of von Willebrand factor (VWF) under shear: it alleviates an inhibitory effect of the VWFA1 domain on cleavage of the A2 domain, 1 and it allows tensile force to be exerted on the A2 domain through at least 2 platelets binding per VWF multimer via the A1 domain (see figure). 2008 Journal Article http://hdl.handle.net/20.500.11937/45221 10.1182/blood-2007-10-116012 American Society of Hematology unknown |
| spellingShingle | Berndt, Michael Andrews, R. Platelet-VWF complexes get the chop |
| title | Platelet-VWF complexes get the chop |
| title_full | Platelet-VWF complexes get the chop |
| title_fullStr | Platelet-VWF complexes get the chop |
| title_full_unstemmed | Platelet-VWF complexes get the chop |
| title_short | Platelet-VWF complexes get the chop |
| title_sort | platelet-vwf complexes get the chop |
| url | http://hdl.handle.net/20.500.11937/45221 |